title: Purification and properties of ferredoxinNAP, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816.
abstract: One of the three components of the naphthalene dioxygenase occurring in induced cells of Pseudomonas sp. strain NCIB 9816 has been purified to homogeneity. The protein contained 2 g-atoms each of iron and acid-labile sulfur and had an apparent molecular weight of 13,600. The evidence indicates that it is a ferredoxin-type protein that functions as an intermediate electron transfer protein in naphthalene dioxygenase activity.
authors.affiliation: Center for Applied Microbiology, University of Texas, Austin 78712.
authors.forename: B E
authors.initials: BE
authors.lastname: Haigler
authors.forename: D T
authors.initials: DT
authors.lastname: Gibson
mesh_terms: D049308:Dioxygenases; D005288:Ferredoxins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000032:analysis*; D010105:Oxygenases / Q000032:analysis*; D011549:Pseudomonas / Q000032:analysis*
chemical_list: D005288:Ferredoxins; D009097:Multienzyme Complexes; D010105:Oxygenases; D049308:Dioxygenases; C038703:naphthalene dioxygenase